Literature DB >> 10329792

Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli.

T Izard1, A Geerlof, A Lewendon, J J Barker.   

Abstract

Phosphopantetheine adenylyltransferase (PPAT, E.C. 2.7.7.3) catalyzes the penultimate step in coenzyme A (CoA) biosynthesis, transferring an adenylyl group from ATP to 4'-phosphopantetheine, and forming dephospho-CoA. Cubic crystals of native PPAT from Escherichia coli as well as PPAT in complex with its substrates were obtained. The crystals belong to space group I23 or I213 with unit-cell dimension a = 135.5 A. The crystals diffract to better than 1.8 A resolution on a Cu Kalpha rotating-anode generator. The asymmetric unit is likely to contain two molecules, corresponding to a packing density of 2.9 A3 Da-1.

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Year:  1999        PMID: 10329792     DOI: 10.1107/s0907444999004394

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  3 in total

1.  A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A.

Authors:  Tina Izard
Journal:  J Bacteriol       Date:  2003-07       Impact factor: 3.490

2.  Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei.

Authors:  Thomas E Edwards; David J Leibly; Janhavi Bhandari; Jacob B Statnekov; Isabelle Phan; Shellie H Dieterich; Jan Abendroth; Bart L Staker; Wesley C Van Voorhis; Peter J Myler; Lance J Stewart
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2011-08-13

3.  Exploiting the anisotropy of anomalous scattering boosts the phasing power of SAD and MAD experiments.

Authors:  Marc Schiltz; Gérard Bricogne
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2008-06-18
  3 in total

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